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Rnd1

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens

RND1
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

2CLS,2REX,3Q3J

Identifiers
AliasesRND1, ARHS, RHO6, RHOS, Rnd1, Rho family GTPase 1
External IDsOMIM:609038;MGI:2444878;HomoloGene:8706;GeneCards:RND1;OMA:RND1 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for RND1
Genomic location for RND1
Band12q13.12Start48,857,145bp[1]
End48,865,870bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for RND1
Genomic location for RND1
Band15|15 F1Start98,561,302bp[2]
End98,575,342bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • vena cava

  • right lobe of liver

  • frontal pole

  • prefrontal cortex

  • right frontal lobe

  • middle temporal gyrus

  • dorsolateral prefrontal cortex

  • primary visual cortex

  • Brodmann area 9

  • cingulate gyrus
Top expressed in
  • lumbar subsegment of spinal cord

  • granulocyte

  • primary visual cortex

  • morula

  • ventricular zone

  • cerebellar cortex

  • superior frontal gyrus

  • endothelial cell of lymphatic vessel

  • neural layer of retina

  • dorsomedial hypothalamic nucleus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

27289

223881

Ensembl

ENSG00000172602

ENSMUSG00000054855

UniProt

Q92730

Q8BLR7

RefSeq (mRNA)

NM_014470

NM_172612

RefSeq (protein)

NP_055285

NP_766200

Location (UCSC)Chr 12: 48.86 – 48.87 MbChr 15: 98.56 – 98.58 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Rnd1 is a small (~21 kDa) signalingG protein (to be specific, aGTPase), and is a member of theRnd subgroup of theRho family of GTPases.[5] It is encoded by the geneRND1.[6]

It contributes to regulating the organization of the actin cytoskeleton in response to extracellular growth factors (Nobes et al., 1998).[supplied by OMIM][6]

Interactions

[edit]

Rnd1 has been shown tointeract withGRB7,[7]PLXNB1,[8]PDE6D,[9][10]ARHGAP5[11] andUBXD5.[12]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000172602Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000054855Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^Ridley AJ (Oct 2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking".Trends in Cell Biology.16 (10):522–9.doi:10.1016/j.tcb.2006.08.006.PMID 16949823.
  6. ^ab"Entrez Gene: RND1 Rho family GTPase 1".
  7. ^Vayssière B, Zalcman G, Mahé Y, Mirey G, Ligensa T, Weidner KM, Chardin P, Camonis J (Feb 2000)."Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family".FEBS Letters.467 (1):91–6.doi:10.1016/S0014-5793(99)01530-6.PMID 10664463.S2CID 4901644.
  8. ^Oinuma I, Katoh H, Harada A, Negishi M (Jul 2003)."Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells".The Journal of Biological Chemistry.278 (28):25671–7.doi:10.1074/jbc.M303047200.PMID 12730235.
  9. ^Nancy V, Callebaut I, El Marjou A, de Gunzburg J (Apr 2002)."The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases".The Journal of Biological Chemistry.277 (17):15076–84.doi:10.1074/jbc.M109983200.PMID 11786539.
  10. ^Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (May 2002)."The complex of Arl2-GTP and PDE delta: from structure to function".The EMBO Journal.21 (9):2095–106.doi:10.1093/emboj/21.9.2095.PMC 125981.PMID 11980706.
  11. ^Wennerberg K, Forget MA, Ellerbroek SM, Arthur WT, Burridge K, Settleman J, Der CJ, Hansen SH (Jul 2003)."Rnd proteins function as RhoA antagonists by activating p190 RhoGAP".Current Biology.13 (13):1106–15.Bibcode:2003CBio...13.1106W.doi:10.1016/S0960-9822(03)00418-4.PMC 6918695.PMID 12842009.
  12. ^Katoh H, Harada A, Mori K, Negishi M (May 2002)."Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers".Molecular and Cellular Biology.22 (9):2952–64.doi:10.1128/MCB.22.9.2952-2964.2002.PMC 133765.PMID 11940653.

Further reading

[edit]
PDB gallery
  • 2cls: THE CRYSTAL STRUCTURE OF THE HUMAN RND1 GTPASE IN THE ACTIVE GTP BOUND STATE
    2cls: THE CRYSTAL STRUCTURE OF THE HUMAN RND1 GTPASE IN THE ACTIVE GTP BOUND STATE
3.6.1
3.6.2
3.6.3-4:ATPase
3.6.3
Cu++ (3.6.3.4)
Ca+ (3.6.3.8)
Na+/K+ (3.6.3.9)
H+/K+ (3.6.3.10)
OtherP-type ATPase
3.6.4
3.6.5:GTPase
3.6.5.1:Heterotrimeric G protein
3.6.5.2:Small GTPase >Ras superfamily
3.6.5.3:Protein-synthesizing GTPase
3.6.5.5-6:Polymerization motors


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